Layh-Schmitt G, Harkenthal M
Hygiene-Institut, Abt. Hygiene und Medizinische Mikrobiologie, Universität Heidelberg, Germany.
FEMS Microbiol Lett. 1999 May 1;174(1):143-9. doi: 10.1111/j.1574-6968.1999.tb13561.x.
After Triton X-100 treatment of Mycoplasma pneumoniae cells, a portion of the adhesin P1 (transmembrane protein) proved to remain tightly associated with the Triton insoluble material (Triton shell) as shown previously by several authors. However, the spontaneous loss of two cytadherence-associated membrane proteins of 90 and 40 kDa (gene product of the open reading frame 6 of the P1 operon) in a hemadsorption-negative mutant, designated M5, resulted in a 100% release of the P1 protein into the Triton phase and in the lack of the characteristic tip-like attachment organelle of M. pneumoniae indicating an essential role of the open reading frame 6 gene product in tip structure formation.
经曲拉通X-100处理肺炎支原体细胞后,如先前几位作者所示,一部分黏附素P1(跨膜蛋白)被证明与曲拉通不溶性物质(曲拉通壳)紧密相关。然而,在一个称为M5的血细胞吸附阴性突变体中,90 kDa和40 kDa的两种与细胞黏附相关的膜蛋白(P1操纵子开放阅读框6的基因产物)自发丢失,导致P1蛋白100%释放到曲拉通相中,且肺炎支原体缺乏特征性的尖端样附着细胞器,这表明开放阅读框6基因产物在尖端结构形成中起重要作用。